Mad Cow Essay Research Paper Who would

Mad Cow Essay, Research Paper

Who would of thought that eating hamburgers, steaks and drinking milk could produce an epidemic disease? These types of food are frequently eaten for their appealing tastes and nutritional values. The discovery of Creutzfeld Jakob Disease (CJD) has been a long and remarkable one. The cause of this disease is a mutated prion protein within the brain that can be either inherited or acquired. These mutations create sponge like holes that destroy the brain. As a result, the disorder gives both behavioural and muscular problems to infected individuals Experiments and discoveries to this disease have led to a further understanding of the diversity of proteins.

In the 1960s, D. Carleton Gadjusek studied the behaviour of a native population in Papua, New Guinea. This population had been eating the brains of dead relatives and as a result, contracted a fatal neurodegenerative disease. When autopsies were taken from the population who died, they appeared to have a distinct pathology. The central brain tissue resembled a sponge with a lot of regions containing microscopic holes. The results of this disease appeared similar to persons affected with CJD.

In 1968, D. Carleton Gadjusek injected an infected biopsy of brain with this disorder into a laboratory animal. As a result, the animal developed this disease. At this time, the biopsy was thought to contain a virus.

At the University of California, Stanley Pruisner and colleagues proposed that agent for this disease was a prion. A prion is a protein version of viruses without the genetic information. Once the prion has entered the body, the normal proteins are mutated. The gene for the normal protein is expressed within normal brain tissue and encodes a protein that resides at the surface of nerve cells. The function is unknown. The mutated prion version of the protein accumulates within nerve cells, forming aggregates that kill cells. The normal protein is soluble in salt solution and is destroyed by protein-eating molecules, known as enzymes. However, the mutated prion protein is insoluble and the protein digestion.

Based on these differences, one might expect these two forms of the prion protein to be composed distinctly different sequences of amino acids, but this is not the case. Prions are proteins, a diverse group of macromolecules. Proteins are capable of a wide variety of functions and activities. This is due to the great variety of structures. Proteins are polymers of amino acids known as polypeptides. These amino acids are the structural building blocks of proteins. Amino acids have a single carbon linked to: an amino group, a carboxylic acid group and a side chain. These side chains vary in structure and determine the chemical properties of the amino acids.

Each protein has a unique and highly ordered structure that is highly specific with the molecules it interacts with. The assortment of the twenty amino acids are important because of the activities the protein can perform in terms of both the intramolecular interactions and intermolecular interactions. Intramolecular interactions are the forces within a molecule. It could be thought of as intramural collegiate activities, interactions within a molecule. Intermolecular interactions could be thought of as intermediate collegiate activities, interactions outside the molecule and this.

During the process of protein synthesis for the normal and mutated prion, special bonds known as peptide bonds form a polypeptide chain. There are several levels of organization that can describe the structure and reactivity of this prion protein. The primary structure is the specific linear sequence of amino acids that constitute the chain. For both the normal and mutated proteins, the primary structure is the same. This sequence of amino acids is very important in both the structure and function of the proteins.

Even though the primary structure of any protein is unique, the secondary structure of many different proteins can be the same. These are selected regions that have protein structures that are repeated throughout the polypeptide chain. In terms of the secondary structure, both the normal and mutated proteins are still the same. With respect to the secondary structure, hydrogen bonding is a very important type of intermolecular force that determines the structure. One type is the alpha helix that is a right-handed coil that is threaded in the same direction as a standard wood screw. The helical structure of a polypeptide results from hydrogen bonds between elements of peptide bonds that are distributed along the backbone of the chain. Another type of is beta-pleated sheet that are completely extended and lie next to one another. They are stabilized by hydrogen bonds between the elements of the peptide linkage.

Tertiary structure of proteins is a result of the folding and twisting of polypeptides through intermolecular interactions. This results in the creation of specific shapes of polypeptide molecules. The intermolecular interactions are a result of hydrogen, ionic and covalent interactions. The chemical nature of side chains on individual amino acid determines how the molecule folds and packs in three dimensions. At this point, this is where the normal and mutated proteins differ in their structure. Moreover, both proteins have the same primary and secondary structure, however, it is